Enhanced pharmacological activity of recombinant human interleukin-11 (rhIL11) by chemical modification with polyethylene glycol

Journal of Controlled Release

Volumn 119, Issue 3, 2007, Pages 271-278

  Takagi, Akira ^a   Yamashita, Noboru ^a   Yoshioka, Tatsunobu ^a   Takaishi, Yuuki ^a   Sano, Kyoko ^a   Yamaguchi, Hideto ^a   Maeda, Atsushi ^a   Saito, Katsumi ^a   Takakura, Yoshinobu ^b   Hashida, Mitsuru ^b  

^a ASTELLAS PHARMA INC   (Japan)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

Plasma duration; Polyethylene glycol, Platelet, Chemical modification; Recombinant human interleukin 11(rhIL11)

Indexed keywords

PERIPHERAL PLATELETS; PHARMACOKINETIC ANALYSIS; PHARMACOLOGICAL ACTIVITY; RECOMBINANT HUMAN INTERLEUKIN;

CHEMICAL MODIFICATION; MOLECULAR WEIGHT; PHARMACOKINETICS; PLASMAS; POLYETHYLENE GLYCOLS;

POLYPEPTIDES;

MACROGOL; MACROGOL 2; RECOMBINANT INTERLEUKIN 11; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ARTICLE; BIOLOGICAL ACTIVITY; CHEMICAL MODIFICATION; CONTROLLED STUDY; DRUG ACTIVITY; DRUG BLOOD LEVEL; DRUG EFFICACY; DRUG MECHANISM; DRUG POTENTIATION; DRUG RETENTION; ENZYME LINKED IMMUNOSORBENT ASSAY; IMMUNOREACTIVITY; MALE; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PRIORITY JOURNAL; THROMBOCYTE COUNT;

ANIMALS; ANTINEOPLASTIC AGENTS; BLOOD PLATELETS; CELL LINE, TUMOR; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG CARRIERS; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; INJECTIONS, INTRAVENOUS; INTERLEUKIN-11; MALE; METABOLIC CLEARANCE RATE; MICE; MICE, INBRED STRAINS; MOLECULAR WEIGHT; PLATELET COUNT; POLYETHYLENE GLYCOLS; RECOMBINANT PROTEINS;

EID: 34248658822     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jconrel.2007.03.009     Document Type: Article

References (38)

1. Du X.X., Keller D., Maze R., and Williams D.A. Comparative effects of in vivo treatment using interleukin-11 and stem cell factor on reconstitution in mice after bone marrow transplantation. Blood 82 (1993) 1016-1022
2. Hagnoc G., Yin T., Cooper S., Schendel P., Yang Y.C., and Broxmeyer H.E. In vivo effects of recombinant interleukin-11 on myelopoiesis in mice. Blood 81 (1993) 965-972
3. Cairo M.S., Plunkett J.M., Nguyen A., Schendel P., and van de Ven C. Effect of interleukin-11 with and without granulocyte colony-stimulating factor on in vivo neonatal rat hematopoiesis: induction of neonatal thrombocytosis by interleukin-11 and synergistic enhancement of neutrophilia by interleukin-11 + granulocyte colony-stimulating factor. Pediatr. Res. 34 (1993) 56-61
4. Yonemura Y., Kawakita M., Masuda T., Fujimoto K., and Takatsuki K. Effect of recombinant human interleukin-11 on rat megakaryopoiesis and thrombopoiesis in vivo: comparative study with interleukin-6. Br. J. Haematol. 84 (1993) 16-23
5. Neben T.Y., Loebelenz J., Hayes L., McCarthy K., Stoudemire J., Schaub R., and Goldman S.J. Recombinant human interleukin-11 stimulates megakaryocytopoiesis and increases peripheral platelets in normal and splenectomized mice. Blood 81 (1993) 901-908
6. Gordon M.S. Thrombopoietic activity of recombinant human interleukin 11 in cancer patients receiving chemotherapy. Cancer Chemother. Pharmacol. 38 (1996) S96-S98
7. Teramura M., Kobayashi S., Yoshinaga K., Iwabe K., and Mizoguchi H. Effect of interleukin 11 on normal and pathological thrombopoiesis. Cancer Chemother. Pharmacol. 38 (1996) S99-S102
8. Orazi R.J., Cooper J., Tong M.S., Gordon L., Battiato G.W., Sledge J.A., Kaye M., Kahsai R., and Hoffman. Effects of recombinant human interleukin-11 (Neumega rhIL-11 growth factor) on megakaryocytopoiesis in human bone marrow. Exp. Hematol. 24 (1996) 1289-1297
9. Tepler L., Elias J.W., Smith M., Hussein G., Rosen A.Y., Chang J.O., Moore M.S., Gordon B., Kuca K.J., Beach J.W., Loewy M.B., Garnick J.A., and Kaye. A randomized placebo-controlled trial of recombinant human interleukin-11 in cancer patients with severe thrombocytopenia due to chemotherapy. Blood 87 (1996) 3607-3614
10. Gordon M.S., McCaskill-Stevens W.J., Battiato L.A., Loewy J., Loesch D., Breeden E., Hoffman R., Beach K.J., Kuca B., Kaye J., and Sledge G.W. A phase I trial of recombinant human interleukin-11 (neumega rhIL-11 growth factor) in women with breast cancer receiving chemotherapy. Blood 87 (1996) 3615-3624
11. Donohue J.H., and Rosenberg S.A. The fate of Interleukin-2 after in vivo administration. J. Immunol. 130 (1983) 2203-2208
12. Tanaka H., and Tokiwa T. Pharmacokinetics of recombinant human granulocyte colony-stimulating factor in the rat by a sandwich enzyme-linked immunosorbent assay. J. Pharmacol. Exp. Ther. 255 (1990) 724-729
13. Bollon A.P., Berent S.L., Torczynski R.M., Hill N.O., Lemeshev Y., Hill J.M., Jia F.L., Joher A., Pichyangkul S., and Khan A. Human cytokines, tumor necrosis factor, and interferons: gene cloning, animal studies, and clinical trials. J. Cell. Biochem. 36 (1988) 353-367
14. Castell J.V., Geiger T., Gross V., Andus T., Walter E., Hirano T., Kishimoto T., and Heinrich P.C. Plasma clearance, organ distribution and target cells of interleukin-6/hepatocyte-stimulating factor in the rat. Eur. J. Biochem. 177 (1988) 357-361
15. Takagi A., Masuda H., Takakura Y., and Hashida M. Disposition characteristics of recombinant human interleukin-11 after a bolus intravenous administration in mice. J. Pharmacol. Exp. Ther. 275 (1995) 537-543
16. Takagi A., Yabe Y., Oka Y., Sawai K., Takakura Y., and Hashida M. Renal disposition of recombinant human interleukin-11 in the isolated perfused rat kidney. Pharm. Res. 14 (1997) 86-90
17. Monfardini C., Schiavon O., Caliceti P., Morpurgo M., Harris J.M., and Veronese F.M. A Branched monomethoxypoly (ethylene glycol) for protein modification. Bioconjug. Chem. 6 (1995) 62-69
18. Yokota H., Kishimoto M., Saito H., Sakai T., Yokota S., and Kojima S. Quantitative in vitro bioassay for recombinant human interleukin-11. J. AOAC Int. 83 (2000) 1053-1057
19. Takagi A., Yamashita, Yoshioka T., Takaishi Y., Nakanishi K., Takemura S., Maeda A., Saito K., Takakura Y., and Hashida M. Incorporation into a biodegradable hyaluronic acid matrix enhances in vivo efficacy of recombinant human interleukin 11 (rhIL11). J. Control. Release 115 (2006) 134-139
20. Tsutsumi Y., Tsunoda S., Kamada H., Kihira T., Nakagawa S., Kaneda Y., Kanamori T., and Mayumi T. Molecular design of hybrid tumour necrosis factor-alpha. II: The molecular size of polyethylene glycol-modified tumour necrosis factor-alpha affects its anti-tumour potency. Br. J. Cancer 74 (1996) 1090-1095
21. Tsutsumi Y., Kihira T., Tsunoda S., Kanamori T., Nakagawa S., and Mayumi T. Molecular design of hybrid tumour necrosis factor alpha with polyethylene glycol increases its anti-tumour potency. Br. J. Cancer 71 (1995) 963-968
22. Maack T., Johnson V., Kau S.T., Figueiredo J., and Sigulem D. Renal filtration, transport, and metabolism of low-molecular-weight proteins: a review. Kidney Int. 16 (1979) 251-270
23. Pettit D.K., Bonnert T.P., Eisenman J., Srinivasan S., Paxton R., Beers C., Lynch D., Miller B., Yost J., Grabstein K.H., and Gombotz W.R. Structure-function studies of interleukin 15 using site-specific mutagenesis, polyethylene glycol conjugation, and homology modeling. J. Biol. Chem. 272 (1997) 2312-2318
24. Chapman A.P., Antoniw P., Spitali M., West S., Stephens S., and King D.J. Therapeutic antibody fragments with prolonged in vivo half-lives. Nat. Biotechnol. 17 (1999) 780-783
25. Tsunoda S., Ishikawa T., Watanabe M., Kamada H., Yamamoto Y., Tsutsumi Y., Hirano T., and Mayumi T. Selective enhancement of thrombopoietic activity of PEGylated interleukin 6 by a simple procedure using a reversible amino-protective reagent. Br. J. Haematol. 112 (2001) 181-188
26. Czupryn M.J., McCoy J.M., and Scoble H.A. Structure-function relationships in human interleukin-11. J. Biol. Chem. 270 (1995) 978-985
27. Miyadai K., Ohsumi J., Yoshimura C., Kawashima I., and Ito Y. Importance of the carboxy-terminus of human interleukin-11 in conserving its biological activity, Bioscience. Biotechnol. Biochem. 60 (1996) 541-542
28. Czupryn M., Bennett F., Dube J., Grant K., Scoble H., Sookdeo H., and McCoy J.M. Alanine-scanning mutagenesis of human interleukin-11: identification of regions important for biological activity. Ann. N.Y. Acad. Sci. 762 (1995) 152-164
29. Du X., and Williams D.A. Interleukin-11: review of molecular, cell biology, and clinical use. Blood 89 (1997) 3897-3908
30. Leary A.G., Zeng H.Q., Clark S.C., and Ogawa M. Growth factor requirements for survival in G0 and entry into the cell cycle of primitive human hemopoietic progenitors. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 4013-4017
31. Tanaka R., Katayama N., Ohishi K., Mahmud N., Itoh R., Tanaka Y., Komada Y., Minami N., Sakurai M., and Shirakawa S. Accelerated cell-cycling of hematopoietic progenitor cells by growth factors. Blood 86 (1995) 73-79
32. Leonard P., Neben T.Y., Kozitza M.K., Quinto C.M., and Goldman S.J. Constant subcutaneous infusion of rhIL-11 in mice: efficient delivery enhances biological activity. Exp. Hematol. 24 (1996) 270-276
33. Kim D.C., Reitz B., Carmichael D.F., and Bloedow D.C. Kidney as a major clearance organ for recombinant human interleukin-1 receptor antagonist. J. Pharm. Sci. 84 (1995) 575-580
34. Brenner B.M., Hostetter T.H., and Humes H.D. Glomerular permselectivity: barrier function based on discrimination of molecular size and charge. Am. J. Physiol. 234 (1978) F455-F460
35. Bailon P., Palleroni A., Schaffer C.A., Spence C.L., Fung W.-J., Porter J.E., Ehrlich G.K., Pan W., Xu Z.-X., Modi M.W., Farid A., Berthold W., and Graves M. Rational design of a potent, long-lasting form of interferon: a 40 kDa branched polyethylene glycol-conjugated interferon-2a for the treatment of hepatitis C. Bioconjug. Chem. 12 (2001) 195-202
36. Yoshioka Y., Tsutsumi Y., Ikemizu S., Yamamoto Y., Shibata H., Nishibata T., Mukai Y., Okamoto T., Taniai M., Kawamura M., Abe Y., Nakagawa S., Nagata S., Yamagata Y., and Mayumi T. Optimal site-specific PEGylation of mutant TNF-alpha improves its antitumor potency. Biochem. Biophys. Res. Commun. 315 (2004) 808-814
37. Morstyn G., Foote M.A., Walker T., and Molineux G. Filgrastim (r-metHuG-CSF) in the 21st century: SD/01. Acta Haematol. 105 (2001) 151-155
38. Yamamoto Y., Tsutsumi Y., Yoshioka Y., Nishibata T., Kobayashi K., Okamoto T., Mukai Y., Shimizu T., Nakagawa S., Nagata S., and Mayumi T. Site-specific PEGylation of a lysine-deficient TNF-α with full bioactivity. Nat. Biotechnol. 21 (2003) 546-552